PLSX_MAGMM
ID PLSX_MAGMM Reviewed; 350 AA.
AC A0L860;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE EC=2.3.1.274 {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Acyl-ACP phosphotransacylase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Acyl-[acyl-carrier-protein]--phosphate acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
DE AltName: Full=Phosphate-acyl-ACP acyltransferase {ECO:0000255|HAMAP-Rule:MF_00019};
GN Name=plsX {ECO:0000255|HAMAP-Rule:MF_00019}; OrderedLocusNames=Mmc1_1644;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
CC -!- FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl-
CC PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme
CC utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
CC {ECO:0000255|HAMAP-Rule:MF_00019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-
CC [ACP]; Xref=Rhea:RHEA:42292, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:14125, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:138651; EC=2.3.1.274; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00019};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBUNIT: Homodimer. Probably interacts with PlsY. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00019}.
CC Note=Associated with the membrane possibly through PlsY.
CC {ECO:0000255|HAMAP-Rule:MF_00019}.
CC -!- SIMILARITY: Belongs to the PlsX family. {ECO:0000255|HAMAP-
CC Rule:MF_00019}.
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DR EMBL; CP000471; ABK44153.1; -; Genomic_DNA.
DR RefSeq; WP_011713301.1; NC_008576.1.
DR AlphaFoldDB; A0L860; -.
DR SMR; A0L860; -.
DR STRING; 156889.Mmc1_1644; -.
DR EnsemblBacteria; ABK44153; ABK44153; Mmc1_1644.
DR KEGG; mgm:Mmc1_1644; -.
DR eggNOG; COG0416; Bacteria.
DR HOGENOM; CLU_039379_1_0_5; -.
DR OMA; HGKSNAR; -.
DR OrthoDB; 631784at2; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000002586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043811; F:phosphate:acyl-[acyl carrier protein] acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR HAMAP; MF_00019; PlsX; 1.
DR InterPro; IPR003664; FA_synthesis.
DR InterPro; IPR012281; Phospholipid_synth_PlsX-like.
DR PANTHER; PTHR30100; PTHR30100; 1.
DR Pfam; PF02504; FA_synthesis; 1.
DR PIRSF; PIRSF002465; Phsphlp_syn_PlsX; 1.
DR TIGRFAMs; TIGR00182; plsX; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..350
FT /note="Phosphate acyltransferase"
FT /id="PRO_1000057175"
SQ SEQUENCE 350 AA; 37666 MW; B277CE0C30D14D99 CRC64;
MTVRIALDAM GGDNAPRAVI EGMLEVQKKR PEVVFTLVGI ESRIRQELEQ MGVEEDGFRI
WHASEVVEMD EKPAVALRTK KDSSMRVGAN LVKENQVDAF VSAGNTGALM ATAKFVLKTL
RGIDRPAIAS VIPAVGGETL MLDLGANVDC SSEHLCQFAL MGSIFANAVL GVRAPRVGLL
NIGEEDTKGN EQVRDAGEQL KARSATLIPG GSYVGNVEGT DIFKDTVDVV VCDGFVGNVS
LKSIEGTAKM LTHYLRGAFT KNWKTKLMYL IARPALRCFR DEMDPRKHNG AILLGLNGVV
VKSHGGADSV AYAHAIHVAV DLAEKQVTKR IRDAVAKFRA EGTQPSDPAV